COAD_METKA
ID COAD_METKA Reviewed; 157 AA.
AC Q8TGY4;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647};
DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00647};
DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00647};
DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647};
DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00647};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00647}; OrderedLocusNames=MK1504;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00647};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00647}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00647}.
CC -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000255|HAMAP-
CC Rule:MF_00647}.
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DR EMBL; AE009439; AAM02717.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TGY4; -.
DR SMR; Q8TGY4; -.
DR STRING; 190192.MK1504; -.
DR EnsemblBacteria; AAM02717; AAM02717; MK1504.
DR KEGG; mka:MK1504; -.
DR PATRIC; fig|190192.8.peg.1662; -.
DR HOGENOM; CLU_035272_5_0_2; -.
DR OMA; FDTLHSG; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00647; PPAT_arch; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR023540; PPAT_arch.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..157
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156321"
SQ SEQUENCE 157 AA; 17612 MW; 7F26ACA3277445F6 CRC64;
MTPLARFRKV VVGGTFDRLH LGHQRLLSVA LELGDRVVIG VTTDSFVREE GKKGVEPFEE
RVRAVRRFVE EKGASDRVEI VPLEDRYGTT LEDDEMDAIV VSPETEPVAL EINELRRKRG
FPPLSIVVIP FVLDGDGRKI SSSRLRGEVD EGPCRDD